1u6g
From Proteopedia
(New page: 200px<br /> <applet load="1u6g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u6g, resolution 3.1Å" /> '''Crystal Structure of...) |
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| - | [[Image:1u6g.gif|left|200px]]<br /> | + | [[Image:1u6g.gif|left|200px]]<br /><applet load="1u6g" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1u6g" size=" | + | |
caption="1u6g, resolution 3.1Å" /> | caption="1u6g, resolution 3.1Å" /> | ||
'''Crystal Structure of The Cand1-Cul1-Roc1 Complex'''<br /> | '''Crystal Structure of The Cand1-Cul1-Roc1 Complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The SCF ubiquitin ligase complex regulates diverse cellular functions by | + | The SCF ubiquitin ligase complex regulates diverse cellular functions by ubiquitinating numerous protein substrates. Cand1, a 120 kDa HEAT repeat protein, forms a tight complex with the Cul1-Roc1 SCF catalytic core, inhibiting the assembly of the multisubunit E3 complex. The crystal structure of the Cand1-Cul1-Roc1 complex shows that Cand1 adopts a highly sinuous superhelical structure, clamping around the elongated SCF scaffold protein Cul1. At one end, a Cand1 beta hairpin protrusion partially occupies the adaptor binding site on Cul1, inhibiting its interactions with the Skp1 adaptor and the substrate-recruiting F box protein subunits. At the other end, two Cand1 HEAT repeats pack against a conserved Cul1 surface cleft and bury a Cul1 lysine residue, whose modification by the ubiquitin-like protein, Nedd8, is able to block Cand1-Cul1 association. Together with biochemical evidence, these structural results elucidate the mechanisms by which Cand1 and Nedd8 regulate the assembly-disassembly cycles of SCF and other cullin-dependent E3 complexes. |
==About this Structure== | ==About this Structure== | ||
| - | 1U6G is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1U6G is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U6G OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Cascio, T | + | [[Category: Cascio, T C.]] |
| - | [[Category: Garbutt, K | + | [[Category: Garbutt, K C.]] |
| - | [[Category: Goldenberg, S | + | [[Category: Goldenberg, S J.]] |
[[Category: Liu, J.]] | [[Category: Liu, J.]] | ||
| - | [[Category: Shumway, S | + | [[Category: Shumway, S D.]] |
[[Category: Xiong, Y.]] | [[Category: Xiong, Y.]] | ||
[[Category: Zheng, N.]] | [[Category: Zheng, N.]] | ||
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[[Category: ring finger]] | [[Category: ring finger]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:21:03 2008'' |
Revision as of 13:21, 21 February 2008
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Crystal Structure of The Cand1-Cul1-Roc1 Complex
Overview
The SCF ubiquitin ligase complex regulates diverse cellular functions by ubiquitinating numerous protein substrates. Cand1, a 120 kDa HEAT repeat protein, forms a tight complex with the Cul1-Roc1 SCF catalytic core, inhibiting the assembly of the multisubunit E3 complex. The crystal structure of the Cand1-Cul1-Roc1 complex shows that Cand1 adopts a highly sinuous superhelical structure, clamping around the elongated SCF scaffold protein Cul1. At one end, a Cand1 beta hairpin protrusion partially occupies the adaptor binding site on Cul1, inhibiting its interactions with the Skp1 adaptor and the substrate-recruiting F box protein subunits. At the other end, two Cand1 HEAT repeats pack against a conserved Cul1 surface cleft and bury a Cul1 lysine residue, whose modification by the ubiquitin-like protein, Nedd8, is able to block Cand1-Cul1 association. Together with biochemical evidence, these structural results elucidate the mechanisms by which Cand1 and Nedd8 regulate the assembly-disassembly cycles of SCF and other cullin-dependent E3 complexes.
About this Structure
1U6G is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases., Goldenberg SJ, Cascio TC, Shumway SD, Garbutt KC, Liu J, Xiong Y, Zheng N, Cell. 2004 Nov 12;119(4):517-28. PMID:15537541
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